Evidence map›Paper›PMID 25224262›Full record

ArticleBiochemistry2014

Skelemin association with αIIbβ3 integrin: a structural model.

Vitaliy Gorbatyuk, Khiem Nguyen, Nataly P Podolnikova, Lalit Deshmukh, Xiaochen Lin, Tatiana P Ugarova, Olga Vinogradova

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 42% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Wdr-1 is essential for F-actin interaction with focal adhesions in platelets.Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Vitaliy GorbatyukDepartment of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut at Storrs , Storrs, Connecticut 06269, United States.
Khiem Nguyen
Nataly P Podolnikova
Lalit Deshmukh
Xiaochen Lin
Tatiana P Ugarova
Olga Vinogradova
University of Connecticut · USArizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the last two decades, our knowledge concerning intracellular events that regulate integrin's affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin αIIbβ3. The model of tertiary assembly is generated based upon NMR data and illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling.

Indexed as

Models, MolecularAnimalsConnectinHumansMicePlatelet Glycoprotein GPIIb-IIIa ComplexProtein Structure, QuaternaryProtein Structure, TertiaryConnectinMyom1 protein, mousePlatelet Glycoprotein GPIIb-IIIa Complex

Identifiers

PMID25224262
PMCPMC4222533
OpenAlexW2418908173

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.